HEADER VIRAL PROTEIN 11-JAN-16 5HIH
TITLE CRYSTAL STRUCTURE OF THE MACRO DOMAIN IN MIDDLE-EAST RESPIRATORY
TITLE 2 SYNDROME CORONAVIRUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ORF1A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: X DOMAIN, RESIDUES 1109-1275;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS;
SOURCE 3 ORGANISM_TAXID: 1335626;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: TUNER PLACI;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS SANDWICH FOLD, NON-STRUCTURAL PROTEIN, MACRODOMAIN, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEI,R.HILGENFELD
REVDAT 5 10-JAN-24 5HIH 1 REMARK
REVDAT 4 06-SEP-17 5HIH 1 REMARK
REVDAT 3 31-AUG-16 5HIH 1 JRNL
REVDAT 2 15-JUN-16 5HIH 1 JRNL
REVDAT 1 20-JAN-16 5HIH 0
JRNL AUTH J.LEI,R.HILGENFELD
JRNL TITL STRUCTURAL AND MUTATIONAL ANALYSIS OF THE INTERACTION
JRNL TITL 2 BETWEEN THE MIDDLE-EAST RESPIRATORY SYNDROME CORONAVIRUS
JRNL TITL 3 (MERS-COV) PAPAIN-LIKE PROTEASE AND HUMAN UBIQUITIN.
JRNL REF VIROL SIN V. 31 288 2016
JRNL REFN ISSN 1995-820X
JRNL PMID 27245450
JRNL DOI 10.1007/S12250-016-3742-4
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 21709
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.143
REMARK 3 R VALUE (WORKING SET) : 0.141
REMARK 3 FREE R VALUE : 0.177
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1111
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.66
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1514
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.52
REMARK 3 BIN R VALUE (WORKING SET) : 0.1660
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.2140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1242
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 186
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.45000
REMARK 3 B22 (A**2) : -1.30000
REMARK 3 B33 (A**2) : 0.84000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.072
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.309
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1296 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1310 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1767 ; 2.292 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3024 ; 1.150 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 178 ; 5.951 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 46 ;38.178 ;25.217
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 230 ;12.843 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ;23.382 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 216 ; 0.128 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1467 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 267 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 679 ; 1.725 ; 1.429
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 678 ; 1.677 ; 1.426
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 850 ; 2.460 ; 2.137
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 851 ; 2.460 ; 2.140
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 617 ; 3.367 ; 1.755
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 618 ; 3.364 ; 1.757
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 912 ; 4.922 ; 2.472
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1613 ; 8.548 ;13.930
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1523 ; 8.216 ;12.882
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5HIH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000217081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-APR-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, DESY
REMARK 200 BEAMLINE : P11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : SI-111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21709
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 52.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 12.30
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2FAV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE, 0.1 M BIS-TRIS PROPANE PH7.0., VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.58500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.38000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.58500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 45.38000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 289 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 ASP A 167
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 321 O HOH A 344 1.71
REMARK 500 O HOH A 233 O HOH A 240 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 14 CB CYS A 14 SG -0.134
REMARK 500 SER A 32 CB SER A 32 OG -0.083
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 98 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 104 CB - CG - OD1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 104 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 LYS A 110 CD - CE - NZ ANGL. DEV. = 14.0 DEGREES
REMARK 500 ARG A 144 CD - NE - CZ ANGL. DEV. = 21.4 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = -10.2 DEGREES
REMARK 500 ARG A 149 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 144 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 5HIH A 1 167 UNP T2BBC3 T2BBC3_9BETC 1109 1275
SEQADV 5HIH GLY A -3 UNP T2BBC3 EXPRESSION TAG
SEQADV 5HIH SER A -2 UNP T2BBC3 EXPRESSION TAG
SEQADV 5HIH HIS A -1 UNP T2BBC3 EXPRESSION TAG
SEQADV 5HIH MET A 0 UNP T2BBC3 EXPRESSION TAG
SEQRES 1 A 171 GLY SER HIS MET ASP PRO LEU SER ASN PHE GLU HIS LYS
SEQRES 2 A 171 VAL ILE THR GLU CYS VAL THR ILE VAL LEU GLY ASP ALA
SEQRES 3 A 171 ILE GLN VAL ALA LYS CYS TYR GLY GLU SER VAL LEU VAL
SEQRES 4 A 171 ASN ALA ALA ASN THR HIS LEU LYS HIS GLY GLY GLY ILE
SEQRES 5 A 171 ALA GLY ALA ILE ASN ALA ALA SER LYS GLY ALA VAL GLN
SEQRES 6 A 171 LYS GLU SER ASP GLU TYR ILE LEU ALA LYS GLY PRO LEU
SEQRES 7 A 171 GLN VAL GLY ASP SER VAL LEU LEU GLN GLY HIS SER LEU
SEQRES 8 A 171 ALA LYS ASN ILE LEU HIS VAL VAL GLY PRO ASP ALA ARG
SEQRES 9 A 171 ALA LYS GLN ASP VAL SER LEU LEU SER LYS CYS TYR LYS
SEQRES 10 A 171 ALA MET ASN ALA TYR PRO LEU VAL VAL THR PRO LEU VAL
SEQRES 11 A 171 SER ALA GLY ILE PHE GLY VAL LYS PRO ALA VAL SER PHE
SEQRES 12 A 171 ASP TYR LEU ILE ARG GLU ALA LYS THR ARG VAL LEU VAL
SEQRES 13 A 171 VAL VAL ASN SER GLN ASP VAL TYR LYS SER LEU THR ILE
SEQRES 14 A 171 VAL ASP
FORMUL 2 HOH *186(H2 O)
HELIX 1 AA1 ASP A 1 PHE A 6 5 6
HELIX 2 AA2 ASP A 21 CYS A 28 1 8
HELIX 3 AA3 GLY A 46 SER A 56 1 11
HELIX 4 AA4 GLY A 58 GLY A 72 1 15
HELIX 5 AA5 ASP A 98 LYS A 102 5 5
HELIX 6 AA6 ASP A 104 SER A 106 5 3
HELIX 7 AA7 LEU A 107 ASN A 116 1 10
HELIX 8 AA8 LYS A 134 ALA A 146 1 13
HELIX 9 AA9 SER A 156 ILE A 165 1 10
SHEET 1 AA1 7 HIS A 8 VAL A 10 0
SHEET 2 AA1 7 VAL A 15 LEU A 19 -1 O ILE A 17 N LYS A 9
SHEET 3 AA1 7 ARG A 149 VAL A 154 1 O VAL A 152 N VAL A 18
SHEET 4 AA1 7 LEU A 120 THR A 123 1 N VAL A 121 O LEU A 151
SHEET 5 AA1 7 VAL A 33 ALA A 37 1 N VAL A 35 O VAL A 122
SHEET 6 AA1 7 ASN A 90 VAL A 94 1 O VAL A 94 N ASN A 36
SHEET 7 AA1 7 SER A 79 GLN A 83 -1 N LEU A 82 O ILE A 91
CRYST1 31.580 65.170 90.760 90.00 90.00 90.00 P 2 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.031666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015344 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011018 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
